We are interested in understanding the molecular basis for cell motility. This is a highly interdisciplinary problem that involves determining how molecular motors in cells convert the chemical energy from ATP hydrolysis into mechanical work. Because the chemical mechanisms of these biological motors are fundamentally different from most motor mechanisms devised by humans, these studies have clear implications for nanotechnology as well as biology.

Our current focus is on studying cooperative interactions among myosin motors in cells. Interestingly, myosin molecules function as force sensors as well as force generators, and so when many myosin molecules function together in ensemble systems like muscle, the force generated by one myosin can cooperative affect the biochemistry of neighboring myosin molecules. To better understand the interplay between myosin’s force generating and force sensing biochemistry, we use state-of-the-art experimental techniques (laser traps, fluorescence microscopy, and single molecule imaging) to measure and systematically perturb (chemically, genetically, and biologically) the mechanics and chemistry of both single myosin motors and collective motor systems. We integrate these results into mathematical and computer models in an effort to better understand the molecular basis for cell motile processes ranging from muscle contraction to intracellular transport.